| Structural highlights
Disease
[LMNA_HUMAN] Defects in LMNA are the cause of Emery-Dreifuss muscular dystrophy type 2, autosomal dominant (EDMD2) [MIM:181350]. A degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] Defects in LMNA are the cause of Emery-Dreifuss muscular dystrophy type 3, autosomal recessive (EDMD3) [MIM:181350]. Defects in LMNA are the cause of cardiomyopathy dilated type 1A (CMD1A) [MIM:115200]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.[14] [15] [16] [17] [18] [19] [20] [21] [22] [23] [24] [25] [26] Defects in LMNA are the cause of familial partial lipodystrophy type 2 (FPLD2) [MIM:151660]; also known as familial partial lipodystrophy Dunnigan type. A disorder characterized by the loss of subcutaneous adipose tissue in the lower parts of the body (limbs, buttocks, trunk). It is accompanied by an accumulation of adipose tissue in the face and neck causing a double chin, fat neck, or cushingoid appearance. Adipose tissue may also accumulate in the axillae, back, labia majora, and intraabdominal region. Affected patients are insulin-resistant and may develop glucose intolerance and diabetes mellitus after age 20 years, hypertriglyceridemia, and low levels of high density lipoprotein cholesterol.[27] [28] [29] [30] [31] [32] [33] [34] Defects in LMNA are the cause of limb-girdle muscular dystrophy type 1B (LGMD1B) [MIM:159001]. LGMD1B is an autosomal dominant degenerative myopathy with age-related atrioventricular cardiac conduction disturbances, dilated cardiomyopathy, and the absence of early contractures. LGMD1B is characterized by slowly progressive skeletal muscle weakness of the hip and shoulder girdles. Muscle biopsy shows mild dystrophic changes.[35] [36] [37] [38] [39] [40] Defects in LMNA are the cause of Charcot-Marie-Tooth disease type 2B1 (CMT2B1) [MIM:605588]. CMT2B1 is a form of Charcot-Marie-Tooth disease, the most common inherited disorder of the peripheral nervous system. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathy or CMT1, and primary peripheral axonal neuropathy or CMT2. Neuropathies of the CMT2 group are characterized by signs of axonal regeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2B1 inheritance is autosomal recessive.[41] Defects in LMNA are the cause of Hutchinson-Gilford progeria syndrome (HGPS) [MIM:176670]. HGPS is a rare genetic disorder characterized by features reminiscent of marked premature aging. Note=HGPS is caused by the toxic accumulation of a mutant form of lamin-A/C. This mutant protein, called progerin, acts to deregulate mitosis and DNA damage signaling, leading to premature cell death and senescence. Progerin lacks the conserved ZMPSTE24/FACE1 cleavage site and therefore remains permanently farnesylated. Thus, although it can enter the nucleus and associate with the nuclear envelope, it cannot incorporate normally into the nuclear lamina.[42] [43] [44] [45] [46] [47] Defects in LMNA are the cause of cardiomyopathy dilated with hypergonadotropic hypogonadism (CMDHH) [MIM:212112]. A disorder characterized by the association of genital anomalies, hypergonadotropic hypogonadism and dilated cardiomyopathy. Patients can present other variable clinical manifestations including mental retardation, skeletal anomalies, scleroderma-like skin, graying and thinning of hair, osteoporosis. Dilated cardiomyopathy is characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Defects in LMNA are the cause of mandibuloacral dysplasia with type A lipodystrophy (MADA) [MIM:248370]. A disorder characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, progeroide appearance, partial alopecia, soft tissue calcinosis, joint contractures, and partial lipodystrophy with loss of subcutaneous fat from the extremities. Adipose tissue in the face, neck and trunk is normal or increased.[48] [49] [50] Defects in LMNA are a cause of lethal tight skin contracture syndrome (LTSCS) [MIM:275210]; also known as restrictive dermopathy (RD). Lethal tight skin contracture syndrome is a rare disorder mainly characterized by intrauterine growth retardation, tight and rigid skin with erosions, prominent superficial vasculature and epidermal hyperkeratosis, facial features (small mouth, small pinched nose and micrognathia), sparse/absent eyelashes and eyebrows, mineralization defects of the skull, thin dysplastic clavicles, pulmonary hypoplasia, multiple joint contractures and an early neonatal lethal course. Liveborn children usually die within the first week of life. The overall prevalence of consanguineous cases suggested an autosomal recessive inheritance.[51] Defects in LMNA are the cause of heart-hand syndrome Slovenian type (HHS-Slovenian) [MIM:610140]. Heart-hand syndrome (HHS) is a clinically and genetically heterogeneous disorder characterized by the co-occurrence of a congenital cardiac disease and limb malformations. Defects in LMNA are the cause of muscular dystrophy congenital LMNA-related (MDCL) [MIM:613205]. It is a form of congenital muscular dystrophy. Patients present at birth, or within the first few months of life, with hypotonia, muscle weakness and often with joint contractures.[52]
Function
[LMNA_HUMAN] Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics.[53] [54] Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence.[55] [56]
Publication Abstract from PubMed
Emerin is a nuclear envelope protein that contributes to genome organization and cell mechanics. Through its N-terminal LAP2-emerin-MAN1 (LEM)-domain, emerin interacts with the DNA-binding protein barrier-to-autointegration (BAF). Emerin also binds to members of the linker of the nucleoskeleton and cytoskeleton (LINC) complex. Mutations in the gene encoding emerin are responsible for the majority of cases of X-linked Emery-Dreifuss muscular dystrophy (X-EDMD). Most of these mutations lead to an absence of emerin. A few missense and short deletion mutations in the disordered region of emerin are also associated with X-EDMD. More recently, missense and short deletion mutations P22L, K37 and T43I were discovered in emerin LEM-domain, associated with isolated atrial cardiac defects (ACD). Here we reveal which defects, at both the molecular and cellular levels, are elicited by these LEM-domain mutations. Whereas K37 mutation impaired the correct folding of the LEM-domain, P22L and T43I had no impact on the 3D structure of emerin. Surprisingly, all three mutants bound to BAF, albeit with a weaker affinity in the case of K37. In human myofibroblasts derived from a patient's fibroblasts, emerin K37 was correctly localized at the inner nuclear membrane, but was present at a significantly lower level, indicating that this mutant is abnormally degraded. Moreover, SUN2 was reduced, and these cells were defective in producing actin stress fibers when grown on a stiff substrate and after cyclic stretches. Altogether, our data suggest that the main effect of mutation K37 is to perturb emerin function within the LINC complex in response to mechanical stress.
An Emerin LEM-Domain Mutation Impairs Cell Response to Mechanical Stress.,Essawy N, Samson C, Petitalot A, Moog S, Bigot A, Herrada I, Marcelot A, Arteni AA, Coirault C, Zinn-Justin S Cells. 2019 Jun 10;8(6). pii: cells8060570. doi: 10.3390/cells8060570. PMID:31185657[57]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
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- ↑ Ostlund C, Bonne G, Schwartz K, Worman HJ. Properties of lamin A mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy. J Cell Sci. 2001 Dec;114(Pt 24):4435-45. PMID:11792809
- ↑ Speckman RA, Garg A, Du F, Bennett L, Veile R, Arioglu E, Taylor SI, Lovett M, Bowcock AM. Mutational and haplotype analyses of families with familial partial lipodystrophy (Dunnigan variety) reveal recurrent missense mutations in the globular C-terminal domain of lamin A/C. Am J Hum Genet. 2000 Apr;66(4):1192-8. PMID:10739751 doi:10.1086/302836
- ↑ Cao H, Hegele RA. Nuclear lamin A/C R482Q mutation in canadian kindreds with Dunnigan-type familial partial lipodystrophy. Hum Mol Genet. 2000 Jan 1;9(1):109-12. PMID:10587585
- ↑ Shackleton S, Lloyd DJ, Jackson SN, Evans R, Niermeijer MF, Singh BM, Schmidt H, Brabant G, Kumar S, Durrington PN, Gregory S, O'Rahilly S, Trembath RC. LMNA, encoding lamin A/C, is mutated in partial lipodystrophy. Nat Genet. 2000 Feb;24(2):153-6. PMID:10655060 doi:10.1038/72807
- ↑ Garg A, Speckman RA, Bowcock AM. Multisystem dystrophy syndrome due to novel missense mutations in the amino-terminal head and alpha-helical rod domains of the lamin A/C gene. Am J Med. 2002 May;112(7):549-55. PMID:12015247
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- ↑ Ki CS, Hong JS, Jeong GY, Ahn KJ, Choi KM, Kim DK, Kim JW. Identification of lamin A/C ( LMNA) gene mutations in Korean patients with autosomal dominant Emery-Dreifuss muscular dystrophy and limb-girdle muscular dystrophy 1B. J Hum Genet. 2002;47(5):225-8. PMID:12032588 doi:10.1007/s100380200029
- ↑ Cenni V, Sabatelli P, Mattioli E, Marmiroli S, Capanni C, Ognibene A, Squarzoni S, Maraldi NM, Bonne G, Columbaro M, Merlini L, Lattanzi G. Lamin A N-terminal phosphorylation is associated with myoblast activation: impairment in Emery-Dreifuss muscular dystrophy. J Med Genet. 2005 Mar;42(3):214-20. PMID:15744034 doi:42/3/214
- ↑ Muchir A, Bonne G, van der Kooi AJ, van Meegen M, Baas F, Bolhuis PA, de Visser M, Schwartz K. Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B). Hum Mol Genet. 2000 May 22;9(9):1453-9. PMID:10814726
- ↑ Kitaguchi T, Matsubara S, Sato M, Miyamoto K, Hirai S, Schwartz K, Bonne G. A missense mutation in the exon 8 of lamin A/C gene in a Japanese case of autosomal dominant limb-girdle muscular dystrophy and cardiac conduction block. Neuromuscul Disord. 2001 Sep;11(6-7):542-6. PMID:11525883
- ↑ Charniot JC, Pascal C, Bouchier C, Sebillon P, Salama J, Duboscq-Bidot L, Peuchmaurd M, Desnos M, Artigou JY, Komajda M. Functional consequences of an LMNA mutation associated with a new cardiac and non-cardiac phenotype. Hum Mutat. 2003 May;21(5):473-81. PMID:12673789 doi:10.1002/humu.10170
- ↑ Rudnik-Schoneborn S, Botzenhart E, Eggermann T, Senderek J, Schoser BG, Schroder R, Wehnert M, Wirth B, Zerres K. Mutations of the LMNA gene can mimic autosomal dominant proximal spinal muscular atrophy. Neurogenetics. 2007 Apr;8(2):137-42. Epub 2006 Nov 29. PMID:17136397 doi:10.1007/s10048-006-0070-0
- ↑ De Sandre-Giovannoli A, Chaouch M, Kozlov S, Vallat JM, Tazir M, Kassouri N, Szepetowski P, Hammadouche T, Vandenberghe A, Stewart CL, Grid D, Levy N. Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse. Am J Hum Genet. 2002 Mar;70(3):726-36. Epub 2002 Jan 17. PMID:11799477 doi:10.1086/339274
- ↑ Haque F, Mazzeo D, Patel JT, Smallwood DT, Ellis JA, Shanahan CM, Shackleton S. Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes. J Biol Chem. 2010 Jan 29;285(5):3487-98. doi: 10.1074/jbc.M109.071910. Epub 2009 , Nov 21. PMID:19933576 doi:10.1074/jbc.M109.071910
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- ↑ Novelli G, Muchir A, Sangiuolo F, Helbling-Leclerc A, D'Apice MR, Massart C, Capon F, Sbraccia P, Federici M, Lauro R, Tudisco C, Pallotta R, Scarano G, Dallapiccola B, Merlini L, Bonne G. Mandibuloacral dysplasia is caused by a mutation in LMNA-encoding lamin A/C. Am J Hum Genet. 2002 Aug;71(2):426-31. Epub 2002 Jun 19. PMID:12075506 doi:S0002-9297(07)60489-3
- ↑ Garg A, Cogulu O, Ozkinay F, Onay H, Agarwal AK. A novel homozygous Ala529Val LMNA mutation in Turkish patients with mandibuloacral dysplasia. J Clin Endocrinol Metab. 2005 Sep;90(9):5259-64. Epub 2005 Jul 5. PMID:15998779 doi:10.1210/jc.2004-2560
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- ↑ Quijano-Roy S, Mbieleu B, Bonnemann CG, Jeannet PY, Colomer J, Clarke NF, Cuisset JM, Roper H, De Meirleir L, D'Amico A, Ben Yaou R, Nascimento A, Barois A, Demay L, Bertini E, Ferreiro A, Sewry CA, Romero NB, Ryan M, Muntoni F, Guicheney P, Richard P, Bonne G, Estournet B. De novo LMNA mutations cause a new form of congenital muscular dystrophy. Ann Neurol. 2008 Aug;64(2):177-86. doi: 10.1002/ana.21417. PMID:18551513 doi:10.1002/ana.21417
- ↑ De Vos WH, Houben F, Hoebe RA, Hennekam R, van Engelen B, Manders EM, Ramaekers FC, Broers JL, Van Oostveldt P. Increased plasticity of the nuclear envelope and hypermobility of telomeres due to the loss of A-type lamins. Biochim Biophys Acta. 2010 Apr;1800(4):448-58. doi: 10.1016/j.bbagen.2010.01.002., Epub 2010 Jan 14. PMID:20079404 doi:10.1016/j.bbagen.2010.01.002
- ↑ Ragnauth CD, Warren DT, Liu Y, McNair R, Tajsic T, Figg N, Shroff R, Skepper J, Shanahan CM. Prelamin A acts to accelerate smooth muscle cell senescence and is a novel biomarker of human vascular aging. Circulation. 2010 May 25;121(20):2200-10. doi: 10.1161/CIRCULATIONAHA.109.902056., Epub 2010 May 10. PMID:20458013 doi:10.1161/CIRCULATIONAHA.109.902056
- ↑ De Vos WH, Houben F, Hoebe RA, Hennekam R, van Engelen B, Manders EM, Ramaekers FC, Broers JL, Van Oostveldt P. Increased plasticity of the nuclear envelope and hypermobility of telomeres due to the loss of A-type lamins. Biochim Biophys Acta. 2010 Apr;1800(4):448-58. doi: 10.1016/j.bbagen.2010.01.002., Epub 2010 Jan 14. PMID:20079404 doi:10.1016/j.bbagen.2010.01.002
- ↑ Ragnauth CD, Warren DT, Liu Y, McNair R, Tajsic T, Figg N, Shroff R, Skepper J, Shanahan CM. Prelamin A acts to accelerate smooth muscle cell senescence and is a novel biomarker of human vascular aging. Circulation. 2010 May 25;121(20):2200-10. doi: 10.1161/CIRCULATIONAHA.109.902056., Epub 2010 May 10. PMID:20458013 doi:10.1161/CIRCULATIONAHA.109.902056
- ↑ Essawy N, Samson C, Petitalot A, Moog S, Bigot A, Herrada I, Marcelot A, Arteni AA, Coirault C, Zinn-Justin S. An Emerin LEM-Domain Mutation Impairs Cell Response to Mechanical Stress. Cells. 2019 Jun 10;8(6). pii: cells8060570. doi: 10.3390/cells8060570. PMID:31185657 doi:http://dx.doi.org/10.3390/cells8060570
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